Dutta, T.; Dutta, A.; Chakraborty, J.; Sarkar, J.; Pal Chowdhury, P.; Gunsalus, I.
Purification and properties of reductase of the three-component p-cymene methyl hydroxylase from Pseudomonas chlororaphis subsp. aureofaciens (2012), Process Biochem., 47, 1263-1267 .
No PubMed abstract available
Cloned(Commentary)
Cloned (Comment) |
Organism |
- |
Pseudomonas chlororaphis subsp. aureofaciens |
Molecular Weight [Da]
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
39000 |
- |
gel fitlration, reductase component CymA |
Pseudomonas chlororaphis subsp. aureofaciens |
Organism
Organism |
UniProt |
Comment |
Textmining |
Pseudomonas chlororaphis subsp. aureofaciens |
P95461 and O84920 and O84919 |
P95461 i.e. reductase subunit CymA, cf. EC 1.8.1.3, O84920 i.e. subunit CymB, O84919 i.e. subunit CymM |
- |
Storage Stability
Storage Stability |
Organism |
70°C, 50 mM potassium phosphate buffer (pH 7.0), 60% glycerol (v/v), subunit CymA is stable for 1 month |
Pseudomonas chlororaphis subsp. aureofaciens |
Subunits
Subunits |
Comment |
Organism |
? |
x * 38433, calculated, x * 38000, SDS-PAGE of reductase component CymA |
Pseudomonas chlororaphis subsp. aureofaciens |
Temperature Stability [°C]
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
30 |
- |
10 min, 42% loss of activity, NADH-cytochrome c reductase activity of subunit CymA |
Pseudomonas chlororaphis subsp. aureofaciens |
50 |
- |
10 min, 98% loss of activity, NADH-cytochrome c reductase activity of subunit CymA |
Pseudomonas chlororaphis subsp. aureofaciens |
pH Optimum
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
8.4 |
- |
NADH-cytochrome c reductase activity of subunit CymA |
Pseudomonas chlororaphis subsp. aureofaciens |
Expression
Organism |
Comment |
Expression |
Pseudomonas chlororaphis subsp. aureofaciens |
expression of subunits CymABM is induced by growth on p-cymene |
up |